Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-7-5
pubmed:abstractText
Regular phospholipid bilayers do not pose efficient barriers for the transport of hydrophobic molecules. The outer membrane (OM) surrounding Gram-negative bacteria is a nontypical, asymmetric bilayer with an outer layer of lipopolysaccharide (LPS). The sugar molecules of the LPS layer prevent spontaneous diffusion of hydrophobic molecules across the OM. As regular OM channels such as porins do not allow passage of hydrophobic molecules, specialized OM transport proteins are required for their uptake. Such proteins, exemplified by channels of the FadL family, transport their substrates according to a lateral diffusion mechanism. Here, substrates diffuse from the lumen of the beta-barrel laterally into the OM, through a stable opening in the wall of the barrel. In this way, the lipopolysaccharide barrier is bypassed and, by depositing the substrates into the OM, a driving force for uptake is provided. Lateral diffusion through protein channel walls also occurs in alpha-helical inner membrane proteins, and could represent a widespread mechanism for proteins that transport and interact with hydrophobic substrates.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-12409203, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-12966144, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-1453953, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-14665678, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-14718163, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-15178802, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-16005205, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-16414958, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-18032007, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-18559855, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-18693753, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-19166984, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-19182779, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-19483784, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-19664953, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-3027089, http://linkedlifedata.com/resource/pubmed/commentcorrection/20533493-356053
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1439-7633
pubmed:author
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1339-43
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Going forward laterally: transmembrane passage of hydrophobic molecules through protein channel walls.
pubmed:affiliation
University of Massachusetts Medical School, Program in Molecular Medicine, 373 Plantation Street, Worcester, MA 01606, USA. bert.vandenberg@umassmed.edu
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural